Anti-DUT / Deoxyuridine triphosphatase

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. DUT Antibody targets Deoxyuridine triphosphatase, encoded by the DUT gene. Deoxyuridine triphosphatase is a highly conserved nucleotide metabolism enzyme that plays a critical role in maintaining genomic integrity by regulating intracellular dUTP levels. The enzyme catalyzes the hydrolysis of dUTP to dUMP and inorganic pyrophosphate, thereby preventing misincorporation of uracil into DNA during replication and repair. This protective function places Deoxyuridine triphosphatase at the center of DNA synthesis fidelity and genome stability control.Functionally, Deoxyuridine triphosphatase acts as a gatekeeper within the thymidylate biosynthesis and DNA replication pathways. By converting dUTP to dUMP, the enzyme simultaneously reduces the pool of potentially mutagenic dUTP and supplies substrate for thymidylate synthase, supporting balanced dTTP production. Loss or inhibition of DUT activity leads to elevated uracil incorporation into DNA, triggering base excision repair pathways and increasing the risk of DNA strand breaks and replication stress. A DUT Antibody is therefore valuable for studies examining DNA replication, nucleotide pool homeostasis, and mechanisms that safeguard genome integrity.Deoxyuridine triphosphatase exists in both nuclear and mitochondrial isoforms generated through alternative targeting sequences, allowing the enzyme to protect genomic DNA as well as mitochondrial DNA from uracil misincorporation. Subcellular localization can vary depending on isoform expression and cellular context, with nuclear localization supporting chromosomal DNA replication and mitochondrial localization contributing to maintenance of mitochondrial genome stability. Expression of DUT is broadly observed in proliferative tissues and dividing cells, reflecting increased demand for nucleotide regulation during DNA synthesis.From a disease relevance perspective, altered regulation of Deoxyuridine triphosphatase has been linked to cancer biology and therapeutic response. Rapidly dividing tumor cells often rely on tight control of nucleotide pools, and DUT expression has been examined in the context of chemotherapeutic sensitivity, particularly for agents that disrupt thymidylate metabolism. Inhibition or dysregulation of DUT can exacerbate DNA damage in cancer cells, while elevated expression may confer resistance to antimetabolite therapies. Beyond oncology, DUT activity is also relevant to viral replication, as several viruses encode or interact with dUTPase enzymes to protect their genomes during replication in host cells.At the molecular level, Deoxyuridine triphosphatase forms a homotrimeric structure that creates a highly specific catalytic pocket for dUTP binding and hydrolysis. The enzyme belongs to the dUTPase family, characterized by conserved motifs required for substrate recognition and catalysis. These structural features are frequently explored in biochemical and structural studies aimed at understanding enzyme regulation and inhibitor design. Antibody-based detection of Deoxyuridine triphosphatase supports research into DNA metabolism, replication stress responses, cancer cell biology, and antiviral mechanisms. NSJ Bioreagents provides reagents intended for research use to support investigations involving DUT expression and function.